Research workbench
Crystal structure of a de novo designed switch protein caging a hemagglutinin binder
Analyse Crystal structure of a de novo designed switch protein caging a hemagglutinin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CBC
- Type
- protein
- Length
- 634 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- De novo designed switch protein caging a hemagglutinin binder (SCAGEHA267_1S)
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 88% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | De novo designed switch protein caging a hemagglutinin binder (SCAGEHA267_1S) | protein | 319 | 88% helix, 0% strand | — |
| B | De novo designed switch protein caging a hemagglutinin binder (SCAGEHA267_1S) | protein | 315 | 89% helix, 0% strand | — |
Ligands and binding sites
- EOH · Ethanol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1144 | 0.76 | 0.79 | 82 | empty |
| 2 | 154 | 0.53 | 0.80 | 23 | empty |
| 3 | 86 | 0.50 | 0.83 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 441 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified, 2 disulfide (engineered, disulfide).
Compared structures
- 7CBC · Crystal structure of a de novo designed switch protein caging a hemagglutinin binder · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 7CBC · PDBe 7CBC
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